Investigation of the structural and functional relationships of oncogene proteins

Proteins are the biomolecular workhorses driving the most biological processes in any living organism. These processes are based on selective interactions between particular proteins. So far the rules governing the coding of the protein's biological function, i.e. its ability to selectively int...

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Bibliographic Details
Published in:Proceedings of the IEEE 2002, Vol.90 (12), p.1859-1867
Main Authors: Pirogova, E., Qiang Fang, Akay, M., Cosic, I.
Format: Article
Language:English
Subjects:
Biochemistry
Biological
Biological processes
Biological system modeling
Biomolecules
Continuous wavelet transform
Continuous wavelet transforms
Digital signal processing
Energy exchange
Fourier transforms
Frequency
Mathematical models
Molecular biophysics
Organisms
Peptides
Position (location)
Proteins
Resonance
Target recognition
Wavelet transforms
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Summary:Proteins are the biomolecular workhorses driving the most biological processes in any living organism. These processes are based on selective interactions between particular proteins. So far the rules governing the coding of the protein's biological function, i.e. its ability to selectively interact with other biomolecules, have not been elucidated The resonant recognition model (RRM) is a novel physicomathematical approach established to analyze the interaction between a protein and its target. The RRM assumes that the specificities of protein interactions are based on the resonant electromagnetic energy transfer at the specific frequency for each interaction. One of the main applications of this model is to predict the location of a protein's biological active site(s) using digital signal processing. This paper incorporates the continuous wavelet transform (CWT) into the RRM to predict the active sites for a chosen protein example. We have investigated the oncogene functional group using digital signal analysis methods, in particular Fourier transform and CWT determined oncogenes' characteristic frequency and functional active sites; and performed the design of the peptide analogous. The results obtained provide new insights into the structure-function relationships of the analyzed oncogene protein family.
ISSN:0018-9219
1558-2256
DOI:10.1109/JPROC.2002.805305